Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2¯ to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2,5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kD each are linked by two cysteines forming an intra-subunit disulfide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kD. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extra-cellular space (7). SOD3 can also be distinguished by its heparinbinding capacity (1).

Catalog #

S8060-09D

Applications

Suitable for use in Western Blot, Immunoprecipitation, ELISA and Immunohistochemistry. Other applications not tested.

Recommended Dilution

Western Blot: 0.5ug/ml was sufficient for detection of Cu/Zn SOD in 20ug of rat brain tissue extract by colorimetric immunoblot analysis using Goat anti-rabbit IgG:AP as the secondary antibody.

Optimal dilutions to be determined by the researcher.

Storage and Stability

May be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.